Literature summary for 2.4.1.41 extracted from

Xu, J.; Morio, A.; Morokuma, D.; Nagata, Y.; Hino, M.; Masuda, A.; Li, Z.; Mon, H.; Kusakabe, T.; Lee, J.M.
A functional polypeptide N-acetylgalactosaminyltransferase (PGANT) initiates O-glycosylation in cultured silkworm BmN4 cells (2018), Appl. Microbiol. Biotechnol., 102, 8783-8797 .

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Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
Golgi apparatus	-	Bombyx mori	5794	-

Organism

Organism	UniProt	Comment	Textmining
Bombyx mori	H9JHA7	-	-

Source Tissue

Source Tissue	Comment	Organism	Textmining
additional information	Pgant2 expresses ubiquitously in silkworm tissues and cultured cells and during development	Bombyx mori	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-N-acetyl-alpha-D-galactosamine + human proteoglycan 4	-	Bombyx mori	UDP + N-acetyl-alpha-D-galactosaminyl-(human proteoglycan 4)	-	?
UDP-N-acetyl-alpha-D-galactosamine + peptide EA2	-	Bombyx mori	UDP + N-acetyl-alpha-D-galactosaminyl-(peptide EA2)	-	?

Synonyms

Synonyms	Comment	Organism
bgibmga008904	-	Bombyx mori
PGANT2	-	Bombyx mori

General Information

General Information	Comment	Organism
physiological function	PGANT2 initiates core 1 O-glycosylation in cultured silkworm BmN4 cells	Bombyx mori

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Release 2023.1 (January 2023)